Phosphatidylinositol (4, 5)-bisphosphate targets double C2 domain protein B to the plasma membrane.

ABSTRACT: Double C2 domain protein B (DOC2B) is a high-affinity Ca²⁺ sensor that translocates from the cytosol to the plasma membrane (PM) and promotes vesicle priming and fusion. However, the molecular mechanism underlying its translocation and targeting to the PM in living cells is not completely understood. DOC2B interacts in vitro with the PM components phosphatidylserine, phosphatidylinositol (4, 5)-bisphosphate [PI(4, 5)P₂ ] and target SNAREs (t-SNAREs). Here, we show that PI(4, 5)P₂ hydrolysis at the PM of living cells abolishes DOC2B translocation, whereas manipulations of t-SNAREs and other phosphoinositides have no effect. Moreover, we were able to redirect DOC2B to intracellular membranes by synthesizing PI(4, 5)P₂ in those membranes. Molecular

SUBMITTER: Michaeli L 

PROVIDER: S-EPMC5967617 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature